In silico docking analysis of piperine with cyclooxygenases

The structure of 1-[5-(1,3-benzodioxol- 5-yl)-1-oxo-2,4-pentadienyl]piperidine (Piperine), C17H19O3N, a versatile bioactive molecule has been redetermined at 100(2) K by X-raycrystallography to explore their potential utilization in inhibition of prostaglandin release. The crystal structure is stabilized by weaknonclassical intermolecular C-H…O hydrogen bonds and also intermolecular C-H…π interactions. The crystallographiccoordinates of the compound were extrapolated to docking studies to elucidate the action of piperine against the enzymes,cyclooxygenases (COX-1 and COX-2) involved in biosynthesis of prostaglandin release. Using AutoDock suite, piperine was docked at the binding site of COX-1 and COX-2 enzyme and a strong affinity (-9.06kcal/mol, Ki =227.73nM and -8.77kcal/mol, Ki = 375.62nM, respectively) was formed by Hydrogen bonds and hydrophobic interactions. These results suggest that piperine can be a promising lead for the development of COX family inhibitors.